Effect of Physicochemical Parameters on the Separation of Proteins from Human Placental Extract by Using a Continuous Foam Fractionating Column
- 1 October 1991
- journal article
- research article
- Published by Taylor & Francis in Separation Science and Technology
- Vol. 26 (10-11) , 1279-1293
- https://doi.org/10.1080/01496399108050532
Abstract
The recovery of valuable proteins (like proteolytic enzymes) from nonconventional biological sources by using modern separation techniques is becoming increasingly important because of their high commercial potential. In the present investigation, isolation of proteins from human placental extract by using the continuous foam fractionation technique is studied. The effect of different physicochemical parameters on the separation of proteins and purification of proteolytic enzymes are reported. A method for finding a quasi-equilibrium relationship between the solute concentration in the foamate and in the effluent by using the same system is described. The quasi-equilibrium curve is also presented.Keywords
This publication has 9 references indexed in Scilit:
- Isolation and purification of protease from human placenta by foam fractionationBiotechnology & Bioengineering, 1987
- Foam separation of DNA and proteins from solutionsBiotechnology & Bioengineering, 1982
- Concentration of proteins by foamingBiotechnology & Bioengineering, 1981
- Laws of Foam Formation and Foam Fractionation. I. The Effect of Different Operating Parameters on the Foam Fractionation of Albumin from a Solution Containing Organic and Inorganic MaterialsSeparation Science, 1975
- Foam Fractionation in a Stripping ColumnSeparation Science, 1972
- Proteases of the genus Bacillus. I. Neutral proteasesBiotechnology & Bioengineering, 1970
- ADSORPTIVE BUBBLE SEPARATION METHODS—Foam Fractionation and Allied TechniquesIndustrial & Engineering Chemistry, 1968
- Foam columns for countercurrent surface—liquid extraction of surface‐active solutesAIChE Journal, 1965
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951